Evidence map›Paper›PMID 23571759›Full record

ArticleNucleic acids research2013

Lif1 SUMOylation and its role in non-homologous end-joining.

Dana Vigasova, Prabha Sarangi, Peter Kolesar, Danusa Vlasáková, Zuzana Slezakova, Veronika Altmannova, Fedor Nikulenkov, Dorothea Anrather, Rainer Gith, Xiaolan Zhao and 2 more

Abstract read
In one paragraph

Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

9 citing papers in PubMed.

  1. Multifaceted roles of SUMO in DNA metabolism.Nucleus (Austin, Tex.) · 2024
    Review
  2. Article
  3. Article
  4. Review
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  7. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors.

Dana VigasovaLaboratory of Molecular Genetics, Cancer Research Institute, Bratislava 83391, Slovak Republic.
Prabha Sarangi
Peter Kolesar
Danusa Vlasáková
Zuzana Slezakova
Veronika Altmannova
Fedor Nikulenkov
Dorothea Anrather
Rainer Gith
Xiaolan Zhao
Miroslav Chovanec
Lumir Krejci

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Nicholas D Socci · 1985 to 2026
$347.4M
The Rtt107 interactome structures and functionsR01GM080670 · NIGMS · SLOAN-KETTERING INST CAN RESEARCH · PI ZHAO, XIAOLAN · 2007 to 2021
$4.5M
NCI NIH HHS P30 CA008748NIGMS NIH HHS R01 GM080670Wellcome Trust WT076476
6 · The paper itself

Abstract

Non-homologous end-joining (NHEJ) repairs DNA double-strand breaks by tethering and ligating the two DNA ends. The mechanisms regulating NHEJ efficiency and interplay between its components are not fully understood. Here, we identify and characterize the SUMOylation of budding yeast Lif1 protein, which is required for the ligation step in NHEJ. We show that Lif1 SUMOylation occurs throughout the cell cycle and requires the Siz SUMO ligases. Single-strand DNA, but not double-strand DNA or the Lif1 binding partner Nej1, is inhibitory to Lif1 SUMOylation. We identify lysine 301 as the major conjugation site and demonstrate that its replacement with arginine completely abolishes Lif1 SUMOylation in vivo and in vitro. The lif1-K301R mutant cells exhibit increased levels of NHEJ repair compared with wild-type cells throughout the cell cycle. This is likely due to the inhibitory effect of Lif1 SUMOylation on both its self-association and newly observed single-strand DNA binding activity. Taken together, these findings suggest that SUMOylation of Lif1 represents a new regulatory mechanism that downregulates NHEJ in a cell cycle phase-independent manner.

Indexed as

DNA End-Joining RepairSumoylationDNADNA-Binding ProteinsDNA Ligase ATPDNA LigasesLysineMutationSaccharomyces cerevisiae ProteinsUbiquitin-Protein LigasesDNADNA-Binding ProteinsDNA Ligase ATPDNA LigasesLIF1 protein, S cerevisiaeLysineNEJ1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSiz1 protein, S cerevisiaeSiz2 protein, S cerevisiaeUbiquitin-Protein LigasesXRS2 protein, S cerevisiae

Identifiers

PMID23571759
PMCPMC3664818

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.